Engineering specific chemical modification sites into a collagen-like protein fromStreptococcus pyogenes
| Autor: | Jerome A. Werkmeister, John A. M. Ramshaw, Yong Y. Peng, Violet Stoichevska, Geoff Dumsday, Aditya V. Vashi |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification 030102 biochemistry & molecular biology Chemistry Metals and Alloys Biomedical Engineering Chemical modification medicine.disease_cause Cyclic peptide Amino acid law.invention Biomaterials 03 medical and health sciences Residue (chemistry) chemistry.chemical_compound 030104 developmental biology Biochemistry law Ceramics and Composites medicine Recombinant DNA Organic chemistry Azide Escherichia coli Cysteine |
| Zdroj: | Journal of Biomedical Materials Research Part A. 105:806-813 |
| ISSN: | 1549-3296 |
| DOI: | 10.1002/jbm.a.35957 |
| Popis: | Recombinant bacterial collagens provide a new opportunity for safe biomedical materials. They are readily expressed in Escherichia coli in good yield and can be readily purified by simple approaches. However, recombinant proteins are limited in that direct secondary modification during expression is generally not easily achieved. Thus, inclusion of unusual amino acids, cyclic peptides, sugars, lipids, and other complex functions generally needs to be achieved chemically after synthesis and extraction. In the present study, we have illustrated that bacterial collagens that have had their sequences modified to include cysteine residue(s), which are not normally present in bacterial collagen-like sequences, enable a range of specific chemical modification reactions to be produced. Various model reactions were shown to be effective for modifying the collagens. The ability to include alkyne (or azide) functions allows the extensive range of substitutions that are available via "click" chemistry to be accessed. When bifunctional reagents were used, some crosslinking occurred to give higher molecular weight polymeric proteins, but gels were not formed. © 2016 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 105A: 806-813, 2017. |
| Databáze: | OpenAIRE |
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